Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential

Detalhes bibliográficos
Autor(a) principal: Carneiro, Rômulo Farias
Data de Publicação: 2017
Outros Autores: Torres, Renato Cézar Farias, Chaves, Renata Pinheiro, Vasconcelos, Mayron Alves de, Sousa, Bruno Lopes de, Goveia, André Castelo Rodrigues, Arruda, Francisco Vassiliepe, Matos, Maria Nágila Carneiro, Matthews-Cascon, Helena, Freire, Valder Nogueira, Teixeira, Edson Holanda, Nagano, Celso Shiniti, Sampaio, Alexandre Holanda
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da Universidade Federal do Ceará (UFC)
Texto Completo: http://www.repositorio.ufc.br/handle/riufc/63573
Resumo: A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms.
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spelling Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potentialSea hareLectinGalacturonic acidBiofilmMass spectrometryA new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms.Marine Biotechnology2022-01-18T19:54:37Z2022-01-18T19:54:37Z2017info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfCARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017.http://www.repositorio.ufc.br/handle/riufc/63573Carneiro, Rômulo FariasTorres, Renato Cézar FariasChaves, Renata PinheiroVasconcelos, Mayron Alves deSousa, Bruno Lopes deGoveia, André Castelo RodriguesArruda, Francisco VassiliepeMatos, Maria Nágila CarneiroMatthews-Cascon, HelenaFreire, Valder NogueiraTeixeira, Edson HolandaNagano, Celso ShinitiSampaio, Alexandre Holandainfo:eu-repo/semantics/openAccessporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFC2023-10-10T19:34:27Zoai:repositorio.ufc.br:riufc/63573Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2024-09-11T18:29:42.908626Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false
dc.title.none.fl_str_mv Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
title Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
spellingShingle Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
Carneiro, Rômulo Farias
Sea hare
Lectin
Galacturonic acid
Biofilm
Mass spectrometry
title_short Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
title_full Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
title_fullStr Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
title_full_unstemmed Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
title_sort Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential
author Carneiro, Rômulo Farias
author_facet Carneiro, Rômulo Farias
Torres, Renato Cézar Farias
Chaves, Renata Pinheiro
Vasconcelos, Mayron Alves de
Sousa, Bruno Lopes de
Goveia, André Castelo Rodrigues
Arruda, Francisco Vassiliepe
Matos, Maria Nágila Carneiro
Matthews-Cascon, Helena
Freire, Valder Nogueira
Teixeira, Edson Holanda
Nagano, Celso Shiniti
Sampaio, Alexandre Holanda
author_role author
author2 Torres, Renato Cézar Farias
Chaves, Renata Pinheiro
Vasconcelos, Mayron Alves de
Sousa, Bruno Lopes de
Goveia, André Castelo Rodrigues
Arruda, Francisco Vassiliepe
Matos, Maria Nágila Carneiro
Matthews-Cascon, Helena
Freire, Valder Nogueira
Teixeira, Edson Holanda
Nagano, Celso Shiniti
Sampaio, Alexandre Holanda
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Carneiro, Rômulo Farias
Torres, Renato Cézar Farias
Chaves, Renata Pinheiro
Vasconcelos, Mayron Alves de
Sousa, Bruno Lopes de
Goveia, André Castelo Rodrigues
Arruda, Francisco Vassiliepe
Matos, Maria Nágila Carneiro
Matthews-Cascon, Helena
Freire, Valder Nogueira
Teixeira, Edson Holanda
Nagano, Celso Shiniti
Sampaio, Alexandre Holanda
dc.subject.por.fl_str_mv Sea hare
Lectin
Galacturonic acid
Biofilm
Mass spectrometry
topic Sea hare
Lectin
Galacturonic acid
Biofilm
Mass spectrometry
description A new lectin from Aplysia dactylomela eggs (ADEL) was isolated by affinity chromatography on HClactivated Sepharose™ media. Hemagglutination caused by ADEL was inhibited by several galactosides, mainly galacturonic acid (Ka = 6.05 × 106 M−1 ). The primary structure of ADEL consists of 217 residues, including 11 halfcystines involved in five intrachain and one interchain disulfide bond, resulting in a molecular mass of 57,228 ± 2 Da, as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. ADEL showed high similarity with lectins isolated from Aplysia eggs, but not with other known lectins, indicating that these lectins could be grouped into a new family of animal lectins. Three glycosylation sites were found in its polypeptide backbone. Data from peptide-Nglycosidase F digestion and MS suggest that all oligosaccharides attached to ADEL are high in mannose. The secondary structure of ADEL is predominantly β-sheet, and its tertiary structure is sensitive to the presence of ligands, as observed by CD. A 3D structure model of ADEL was created and shows two domains connected by a short loop. Domain A is composed of a flat three-stranded and a curved five-stranded βsheet, while domain B presents a flat three-stranded and a curved four-stranded β-sheet. Molecular docking revealed favorable binding energies for interactions between lectin and galacturonic acid, lactose, galactosamine, and galactose. Moreover, ADEL was able to agglutinate and inhibit biofilm formation of Staphylococcus aureus, suggesting that this lectin may be a potential alternative to conventional use of antimicrobial agents in the treatment of infections caused by Staphylococcal biofilms.
publishDate 2017
dc.date.none.fl_str_mv 2017
2022-01-18T19:54:37Z
2022-01-18T19:54:37Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv CARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017.
http://www.repositorio.ufc.br/handle/riufc/63573
identifier_str_mv CARNEIRO, Rômulo Farias et al. Purification, biochemical characterization, and amino acid sequence of a novel type of lectin from Aplysia dactylomela eggs with antibacterial/antibiofilm potential. Marine Biotechnology, [s. l.], v. 19, p. 49-64, 2017.
url http://www.repositorio.ufc.br/handle/riufc/63573
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Marine Biotechnology
publisher.none.fl_str_mv Marine Biotechnology
dc.source.none.fl_str_mv reponame:Repositório Institucional da Universidade Federal do Ceará (UFC)
instname:Universidade Federal do Ceará (UFC)
instacron:UFC
instname_str Universidade Federal do Ceará (UFC)
instacron_str UFC
institution UFC
reponame_str Repositório Institucional da Universidade Federal do Ceará (UFC)
collection Repositório Institucional da Universidade Federal do Ceará (UFC)
repository.name.fl_str_mv Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)
repository.mail.fl_str_mv bu@ufc.br || repositorio@ufc.br
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